GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
You don't have sufficient rights on this wiki to edit tables. Perhaps you need to log in. Changes you make in the Table editor will not be saved back to the wiki
Richie, CT, Bembenek, JN, Chestnut, B, Furuta, T, Schumacher, JM, Wallenfang, M and Golden, A (2011) Protein phosphatase 5 is a negative regulator of separase function during cortical granule exocytosis in C. elegans. J. Cell. Sci. 124:2903-13
Mutations in the Caenorhabditis elegans separase gene, sep-1, are embryonic lethal. Newly fertilized mutant embryos have defects in polar body extrusion, fail to undergo cortical granule exocytosis, and subsequently fail to complete cytokinesis. Chromosome nondisjunction during the meiotic divisions is readily apparent after depletion of sep-1 by RNAi treatment, but much less so in hypomorphic mutant embryos. To identify factors that influence the activity of separase in cortical granule exocytosis and cytokinesis, we carried out a genetic suppressor screen. A mutation in the protein phosphatase 5 (pph-5) gene was identified as an extragenic suppressor of sep-1. This mutation suppressed the phenotypes of hypomorphic separase mutants but not RNAi depleted animals. Depletion of pph-5 caused no phenotypes on its own, but was effective in restoring localization of mutant separase to vesicles and suppressing cortical granule exocytosis and cytokinesis phenotypes. The identification of PPH-5 as a suppressor of separase suggests that a new phospho-regulatory pathway plays an important role in regulating anaphase functions of separase.
Alleles; Animals; Caenorhabditis elegans/enzymology; Caenorhabditis elegans/genetics; Caenorhabditis elegans/metabolism; Caenorhabditis elegans Proteins/genetics; Caenorhabditis elegans Proteins/metabolism; Cell Cycle Proteins/genetics; Cell Cycle Proteins/metabolism; Cytokinesis/genetics; Cytoplasmic Granules/genetics; Cytoplasmic Granules/metabolism; Endopeptidases/genetics; Endopeptidases/metabolism; Exocytosis/physiology; Mutation; Nuclear Proteins/biosynthesis; Nuclear Proteins/deficiency; Nuclear Proteins/genetics; Nuclear Proteins/metabolism; Phosphoprotein Phosphatases/biosynthesis; Phosphoprotein Phosphatases/deficiency; Phosphoprotein Phosphatases/genetics; Phosphoprotein Phosphatases/metabolism